1. description of the discipline
TRANSCRIPT
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1. Description of the discipline Biochemistry of Animals with the Fundamentals of Fhysical and Colloidal Chemistry ___________________________________________________________________
(name)
Field of knowledge, direction of training, specialty, education and qualification level
Education Degree «Master» Direction of training «Veterinary Medicine» Specialty 211- «Veterinary Medicine»
Specialization
Characteristics of discipline
Kind Regulatory
Total hours 180
Number of ECTS credits 6
Number of thematic modules 6
Course project (work) (if it is in the working educational plan)
-
Form of control Test, Exam
Indicators discipline for full-time and extramural study
full-time study extramural study
Year of training 2
Semester
Lectures 60 hours
Practical classes, seminars - hours
Laboratory classes 75 hours
Self-work 45 hours
Self-work under supervising tutor - hours
Number of weekly hours
for full-time study:
classroom
self-work of student −
5 hours
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"Biochemistry of Animals with the Fundamentals of Physical and Colloidal
Chemistry" is a mandatory component of the educational program "Veterinary
Medicine", which provides basic concepts about the chemical composition of the
animal, classification, functions of proteins, carbohydrates, lipids, minerals, enzymes,
hormones and vitamins. The main ways of biochemical processes that provide
homeostasis, energy balance, growth and development of animals are subject to study.
Significant attention is paid to the study of the biochemical composition of biological
fluids and tissues of animals and the processes that occur in them.
The study of the discipline " Biochemistry of Animals with the Fundamentals of
Physical and Colloidal Chemistry " provides mastery of such general competencies as
knowledge and understanding of the subject area, the ability to search, process and
analyze information from various sources, the ability to apply knowledge in practical
situations.
Studying the discipline "Biochemistry of Animals with the Fundamentals of
Physical and Colloidal Chemistry" provides the acquisition of such professional
competencies as the ability to use modern knowledge of the laws of biochemistry of
different species to effectively adjust the treatment of animals and drugs.
2. The purpose and tasks discipline
The purpose of "Biochemistry of Animals with the Fundamentals of Physical and
Colloidal Chemistry" is to equip students by complete system of knowledge about the
chemical composition of living organisms, physico-chemical and biological properties
of natural compounds, the main pathways of metabolism, regulatory mechanisms and
the relationship of metabolic processes that is to take on theoretical fundamentals of
metabolic transformations and their regulation in animals and practical skills of their
study.
Tasks of the course "Biochemistry of Animals with the Fundamentals of Physical
and Colloidal Chemistry" are to learn the basics of life organisms, namely: structure,
physico-chemical and biological properties of substances and their metabolism and its
regulation and metabolic changes using as feed and as medicines to promote health and
improve animal productivity.
After study of the discipline, the student must
know:
- chemical fundamentals of life organisms, including chemical structure and
properties of natural compounds and their complexes, major pathways and mechanisms
of regulation of metabolism, biochemical mechanisms of realization of genetic
information;
- theoretical and practical importance of biochemistry and its relationship with
other natural sciences;
- the latest achievements of biochemistry and prospects for their use in various
sectors of the national economy, especially in veterinary medicine;
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be able: to orientate in biochemical studies at the present level, namely: to choose
the appropriate physico-chemical and biochemical methods and methodological
approaches and equipment, select biological samples, possess conventional methods of
determination in biological objects of various metabolites, indexes with devices
biochemical laboratory for characteristics of the physiological state of animals, and its
changes.
Acquisition of competencies:
- study of the discipline "Biochemistry of Animals with the Fundamentals of
Physical and Colloidal Chemistry" provides mastery of such general competencies as
knowledge and understanding of the subject area, the ability to search, process and
analyze information from various sources, the ability to apply knowledge in practical
situations;
- the study of the discipline "Biochemistry of Animals with the Fundamentals of
Physical and Colloidal Chemistry" provides mastery of such professional competencies
as the ability to use modern knowledge of the laws of biochemistry of different species
of animals to effectively manage the treatment of animals and drugs.
3. The program and structure of study discipline:
– full-time study;
Thematic Module 1. Fundamentals of Physical and Colloidal Chemistry
Theme of lecture lesson 1. Animal biochemistry is the history of its development
and its place among the natural sciences.
Biochemistry. History of biochemistry as a science. Biochemistry is a science of
the origin and development of life. Connection with related and applied sciences. The
place of biochemistry as a discipline in the system of biological education and its
significance for veterinary medicine. Modern problems and prospects of biochemistry
development (introductory lecture).
Theme of lecture lesson 2. Fundamentals of Physical Chemistry (1,2,3)
Subject and methods of physical chemistry. pH, value for the body. pH scale.
Communication length and energy. Types of physicochemical interactions in the matter:
chemical, physical. Hydrogen bond.
Intermolecular interactions. The physical state of substances. Gases are perfect
and real. Gas laws, their significance for understanding the processes of gas exchange in
the body. Boiling and evaporation of substances.
Buffer solutions, their components. Blood buffer systems. Solutions.
Classification. Characteristics of the acid-base state of the organism. Diffusion.
Osmosis. Osmotic pressure. Oncotic pressure.
Fundamentals of Physical Chemistry (2)
Theories of solutions; Dilution of solutions; Solvates; Hypotonic, hypertonic and
isotonic solutions; Erythrocytes hemolysis and plasmolysis. Sorption, sorption kinds.
Chemical and physical nature of sorption. Adsorption, types of adsorption.
Surfactants (Surface active agents). Sorption in biological phenomena, its
significance. Chromatographic and electrophoretic methods for the separation of
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macromolecular materials. Viscosity. Dynamic viscosity, internal friction. Fluidness of
liquids.
Fundamentals of Physical Chemistry (3)
Equilibrium in the system of solution–vapour. Raul’s Laws. Measurement of
osmotic pressure by methods of cryoscopy and ebullioscopy. Dispersed systems, their
classification.
Surface phenomena in the dispersed systems. Surface strain, surface energy.
Theme of lecture lesson 3. Fundamentals of Colloidal Chemistry (1)
Subject and methods of colloidal chemistry. Colloidal solutions, their
characteristics. Molecular-kinetic properties of colloidal solutions. Electrokinetic
properties of solutions. Kinetic and aggregative resilience of colloidal solutions.
Coagulation.
Syneresis. Sols. Molecular and kinetic properties of sols.
Fundamentals of Colloidal Chemistry (2)
Structure of colloidal particle. Iso-electric state of colloidal systems. Colloidal
protection. Dispersed Systems Usage in Veterinarian Medicine. Optical properties of
sols.
Methods for sol preparation. Purification of colloidal solution by dialysis,
electrical dialysis, adsorbent. Aerosol. Gels, characteristics, classification, properties.
Thematic Module 2. Physico-chemical methods of research in biochemistry
Theme of lecture lesson 1. Physico-chemical methods of research in biochemistry
(1)
Physical and chemical fundamentals of spectral analysis (spectrophotometric and
colour-metric methods). Physical and chemical phenomena in a base of
chromatography, electrophoresis (for example, sequenceing of high molecular
substances: amino acids, nucleic acids).
Solution concentration determination.
Physical-chemical methods of research in biochemistry (2)
Biosubstances and their chemical composition as objects of biochemical research,
nutrient media, and preparative methods.
Selection of objects of biochemical research (for example, on energy value). The
purpose of use of a medium. Homogenization. Examples of preparative methods
(centrifugation). Obtaining cell compartments.
Thematic Module 3. Biochemistry: Statics
Theme of lecture lesson 1. Cell and its organic compounds. Carbohydrates (1)
General characteristics. Mono-, oligo-, polysaccharides. Glycosidic bond, types of
bonds. Study of chemical properties of sucrose, lactose, starch.
Laboratory simplified tests for carbohydrates.
Cell and its organic compounds. Carbohydrates (2)
Homopolysaccharides. Heteropolysaccharides. Functions and biological
importance of carbohydrates in the organism.
The functions of biological membranes and the role of carbohydrates as their
structural elements. Membrane structures of animal cells.
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Theme of lecture lesson 2. Lipids and biomembranes (1, 2)
Simple and complex lipids. Simple lipids: acyl glycerols, waxes (the main
representatives). General characteristics: structure, physico-chemical properties and
functional role. Fatty acids (saturated, mono- and polyenes), their physical and chemical
properties. Eicosanoids (structure and function). Alcohols as components of simple
lipids.
Lipids that colud be saponificated. Surface-active properties of soap.
Complex lipids: general characteristics, structure, composition, biological
significance. Phospholipids (glycerophospholipids and sphingophospholipids),
glycolipids (glicosylglycerols and glycosylsphingolipids), their main representatives.
Lipids that colud not be saponificated: terpenes (terpenes derivatives - carotenes
and vitamin A, vitamin E) and steroids (the structure and properties of some
representatives: cholesterol, bile acids, steroid hormones, vitamin D).
Theme of lecture lesson 3. Amino acids, peptides, proteins (1, 2)
Amino acids: general characteristics, classification. Non-essential and essential
amino acids. The biological significance.
Methods for determination of amino acids. Ninhydrine reaction on amino acids.
Proteins: Classification of proteins, the chemical composition of proteins. Simple
and complex proteins. Simple proteins: structure, properties, functions, individual
members and their role.
Methods of isolation of proteins. Fractionation of proteins.
Amino acids, peptides, proteins (3)
Conjugated proteins: structure, properties and biological role chromo-proteins
(flavo-proteins and hemoproteins), glycoproteins, lipoproteins, metalo-proteins,
phospho-proteins and nucleoprotein. The functional role of individual proteins.
Nitrogen balance in animals. Total, protein, non-protein Nitrogen.
Theme of lecture lesson 4. Nucleosides, nucleotides and nucleic acids (NA)
Nucleosides, nucleotides, NA. Spreading and localization in the biological objects, their
composition and biological role. Nitrogen containing bases. Carbohydrate components.
Chemical structure, function and use of nucleosides and nucleotides. General
characteristics of DNA and RNA.
Condition of nucleic acids in the cell.
Structure and properties of DNA and RNA. Structural organization of oligo- and
polynucleotides. Characterization of the primary structure of DNA. Double-stranded
DNA, the bonds that stabilize the structure of DNA. The principle of complementarity.
Single and double stranded DNA. Structure, properties and functions of messenger,
transport and ribosomal RNA. Physico-chemical properties of DNA and RNA.
Molecular organization of nuclear chromatin and ribosomes.
Thematic Module 4. Regulatory effects of inorganic and organic substances on the
metabolism
Theme of lecture lesson 1. Water and mineral balance and its effect on the
metabolism
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Subject and tasks of biochemistry. Contribution of the Ukrainian biochemists to the
development of biochemistry. Water, its exchange and state in the organism. Sorption.
Regulation. Abnormal states of water’s exchange.
Quantity elements (macroelements) and essential trace elements (microelements).
Biochemical functions of inorganic substances.
Electrolyte balance of organisms. Regulation and abnormal states of mineral
turnover.
Theme of lecture lesson 2. Vitamins. Coenzymes
Regulators of metabolism: vitamins. Common characteristcs. Vitaminology. Fat-
soluble vitamins: A and D with their vitamers, E, K, and F. Water-soluble vitamins: for
example, В1 (thiamine); В2 (riboflavin); В3 (pantothenic acid); В5 (nicotin amide або
vitamin РР); В6 (pyridoxal, pyridoxine, pyridoxamine or vitamin B6); В7or8 (Н or biotin);
В9 (Вс or folic acid), В12 (cyanocobalamin).
Precursors of vitamins (carotinoides - precursor of vitamin А). Sources of
vitamins. Vitamin-like substances: inositol; vitamin В4 (choline); vitamin В11, (Вт,
carnitine); vitamin В13 (orotic acid); vitamin В15 (пангамова acid); p-aminobensoic acid
(PABA). Antivitamins. Avitaminosis, hypo- and hypervitaminosis of farm animals.
Coenzymes (thiamine diphosphate, FAD, FMN, Coenzym А, NAD, NADP,
pyridoxal phosphate, biocytin, lipoamides, 5’-deoxyadenosylcobalamin, methyl
cobalamin) and their role in catalytic processes under action of enzymes.
Theme of lecture lesson 3. Enzymes and their kinetic properties
Common information concerning enzymes: structure, definition of substrate,
active center, enzyme-substrate complex, substrate specificity. Cofactors and
coenzymes. Equation of enzymatic reaction. Mechanism of enzymatic reaction with one
substrate. Enzyme numbers and their classification. The enzyme classes: 1) oxido-
reductase, 2) transferase, 3) hydrolase, 4) lyase, 5) isomerase, 6) ligase, and typical
reactions for enzymes of each class.
The terms those are used in enzymology. Enzyme kinetics. Influence of physical
and chemical factors on enzymatic activity. Activators and inhibitors of enzymes.
Theme of lecture lesson 4. Hormones and mechanisms of their influence on
metabolic processes
Regulators of metabolism: hormones. General characteristics.
Structure of molecules, biosynthesis, metabolism. Types of communication
between cells (direct contact, neurotransmitters, and endocrine signaling molecules).
Depending on the speed of the signals those are distinguished on the following types of
signaling: for neurotransmitters, it occurs and is extinguished in milliseconds signal, the
receptor proteins which are ion channels postsynaptic membrane; for protein and
peptide nature hormones, catecholamines, prostaglandins, signal transmission takes
minutes and its receptors located on the plasma membrane; for steroid and thyroid
hormone, signaling occurs over hours, days and they are perceived receptors in the
cytosol and nucleus.
Mechanisms of hormonal influence on metabolic processes.
Thematic Module 5. Dynamic and functional biochemistry
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Theme of lecture lesson 1. Biochemistry of digestion and features of digestive
processes in different organisms
Biochemistry of digestion. Cavity, parietal, membrane, cellular digestion.
Biological features of absorption of substances. Features of protein digestion in
ruminants, transformation of Nitrogen-containing non-protein substances. Digestive
hormones (gastrin, secretin, cholecystokinin, gastric inhibitor peptide and motylin). The
formation of hydrochloric acid. Transmembrane transport of substances: simple
diffusion, passive transport (facilitated and exchange diffusion), active transport
(primary and secondary transport) endocytosis and exocytosis. Two types of
endocytosis: phagocytosis and pinocytosis. Mechanisms of transport.
Digestion of nutrients (proteins, carbohydrates, nucleic acids, lipids, vitamins and
inorganic substances, cellulose), enzyme hydrolysis (hydrolysis products: amino acids,
monosaccharides, nitrogenous bases, pentose, phosphate, nucloeside, 2-monoacyl
glycerol, FA, cholesterol, cellulose, lignin), re-sorbtion (hydrophilic and lipophilic
substances), or transport through the blood to the liver, portal vein, lymphatic system.
Digestive enzymes of proteins, carbohydrates, nucleic acids, lipids. Features of
digestion in newborns.
Theme of lecture lesson 2. Metabolism of carbohydrates and its peculiarities (in
ruminants) (1)
Carbohydrate metabolism. Intermediary carbohydrate metabolism in the organs
and tissues. Anaerobic decomposition of carbohydrates - glycolysis (its stages,
reversible and irreversible reactions, and regulation), glycogenolysis. Regulatory
enzymes of glycolysis. Pasteur Effect (inhibition of glycolysis reactions in conditions of
activation of cellular respiration). The value of anaerobic glycolysis.
The pathways of glucose transformation. Glucose-lactate cycle (cycle Corey).
Metabolic conversion of glucose-6-phosphate in erythrocytes. Glycolysis and
glycogenolysis in different states of the organism and the ways of their correction.
Hypo-and hyperglycemia.
Metabolism of carbohydrates and its peculiarities (in ruminants) (2)
Peculiarities of carbohydrate metabolism in ruminants. Pentose phosphate
(phosphogluconate) pathway (PPP): its stages and their functioning (including
erythrocytes). The biological significance of PPP. Hereditary deficiency of glucose-6-
phosphate dehydrogenase (enzyme PPP) causing hemolysis of erythrocytes.
Synthesis of glucose, glycogen, lactose.
Gluconeogenesis, characterization bypass reactions of glycolysis and its hormonal
regulation (including insulin, glucagon, epinephrine and glucocorticoids). Glucose-
lactate cycle (cycle Corey). Glucose-alanine cycle.
Propionate (product of carbohydrate metabolism by microorganisms) - the main
substrate of gluconeogenesis in ruminants.
Glucogenous amino acids. Cooperation between glycolysis and gluconeogenesis.
Effect of antagonistic hormones (insulin and glucagon) and hormone-synergists
(glucagon, epinephrine, corticosteroids, somatropin) on carbohydrate metabolism.
Glycogenesis, synthesis of lactose in the lactating mammary gland and non-
lactating tissues.
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Theme of lecture lesson 3. Amphibolic transformation of organic substances (the
tricarboxylic acids cycle). Energy of biochemical processes
The tricarboxylic acids cycle (TCAC or citric acid cycle, or Krebs’ cycle) TCAC:
enzymes and sequence of reactions. Reduction of NAD and FAD, phosphorylation on
the level of substrate. Energy balance of TCAC. Usage of metabolities of TCAC in
metabolism of carbohydrates, lipids, amino acids, proteins, nucleic acids and their
components (common characteristics).
Biological oxidation, types of biological oxidation.
The modern theory of tissue respiration. The theory of oxidative phosphorylation.
Main macroergic compounds. Oxidation coupled with phosphorylation of ADP
(substrate and oxidative phosphorylation). Principles of structural and functional
organization of electron transport (respiratory) chain of mitochondria. NAD-and NADP-
dependent dehydrogenase flavin enzymes, ubiquinone, cytochromes and cytochrome
oxidase. Mechanisms of coupling of oxidation and phosphorylation in the respiratory
chain.
Transmembrane potential of protons, ATP synthase work.
Theme of lecture lesson 4. Metabolism of lipids (1)
Exchange of lipids. Lipid digestion and absorption of the products of their
hydrolysis. Role of bile acid in digestion of lipids. Intermediate lipid metabolism in the
organs and tissues. Transportation forms of lipids (lipoprotein complexes) functions
apo-proteins. Lipolysis (catabolism) of TAG. The molecular basis for the regulation of
adipocyte triacyl glycerol lipase activity - its covalent modification by reversible
phosphorylation-dephosphorylation.
Adenilate cyclase mechanism for the regulation of lipolysis. Hormonal regulation
of lipolysis. Catabolism of phospholipids sterides. Ketonogenesis (formation of ketone
bodies: acetone, aceto acetate, beta-hydroxybutyrate). Reactions of utilization of ketone
bodies. Metabolism of ketone bodies in pathological conditions.
Metabolism of lipids (2)
Exchange of glycerol and fatty acids (FA). β-oxidation of FA (sequence of
reactions and their localization) and its energy. Oxidation of unsaturated fatty acids.
Oxidation FA with an odd number of carbon atoms. β-oxidation FA (C20 and more than
20 carbon in the Carbon-chain of FA). α-and ω-oxidation of FA. Cleavage of branched
of FA during α-oxidation. ω oxidation (as detoxification of intermediates of defective β-
oxidation) in the smooth endoplasmic reticulum of liver. Oxidation of glycerol and its
energy. Coordinated regulation of metabolism of FA. Synthesis of FA (role
multienzyme complex).
Elongation of the saturated FA. Formation of the unsaturated FA. Metabolic
pathways of biosynthesis of saturated and unsaturated FA by enzyme systems in the
organism. The formation of glycerol. Lipogenesis is the synthesis of neutral fats
(triacylglycerols, TAG). Ways of TAG synthesis and phospholipids.
Theme of lecture lesson 5. The metabolic processes of proteins and some amino
acids (1)
Biochemistry of proteins. Proteins complete and defective on essential amino
acids. The biological value of proteins. Essential amino acids. Exchange of some amino
acids. Absorption of amino acids. Digestion of proteins. Enzymes of digestion of
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proteins. Proteolysis and proteolytic enzymes. Predecessors of proteolytic enzymes
(trypsinogen, himotrypsynohen, proelastase). Intracellular proteolysis of proteins in
lysosomes. Degradation of proteins in proteasome which is localized in the cytoplasm.
Proteins decay in colon and disposal processes of generated toxic products. The
formation of the end products of protein metabolism (H2O, CO2, NH3). Ways of removal
of ammonia. Ornithine cycle of formation of urea. Abnormality of the urea cycle
formation cause disorders such as argininemia.
Common ways of converting amino acids. Reactions of conversion of amino
acids: deamination, decarboxylation, transamination of amino acids (aspartate
aminotransferase or AST and alaninaminotransferase or ALT). Biochemical value of
conversion of amino acids.
Protein synthesis. Synthesis of somel amino acids, peptides (insulin, glucagon,
glutathione) and protein. Nitrogen balance in the body is primarily determined by the
metabolism of protein. Protein biosynthesis (translation) and its stages (initiation,
elongation, termination). Translation in prokaryotes and eukaryotes. Effect of antibiotics
on the process of protein synthesis. Synthesis of insulin. Effect of insulin on glucose
uptake by the cell and on metabolism glucose. Synthesis of glutathione and its
antioxidant role.
Synthesis of amino acids through transamination reactions: pyruvate (glycolytic
end-product) in alanine; oxaloacetate (intermediate of TCAC) in aspartate, and alpha-
ketoglutarate (intermediate of TCAC) in glutamate. Synthesis of glycine and role of
tetrahydrofolate.
Theme of lecture lesson 6. Catabolism and anabolism of nucleotides and nucleic
acids (1)
Catabolic processes of nucleic acids (NA). Exchange of nucleic acids.
Nucleoprotein digestion, absorption of hydrolysis products. Effect of antibiotics on
nucleoproteins. Enzymes of hydrolysis of NA (endonuclease and exonuclease). The
specificity of nucleases: RNase, DNAase, non-specific nucleases. 3'-and 5'-nuclease.
The decay of NA in tissues. Catabolism of purine or synthesis or uric acid and
allantoin. Hyperuricemia (gout). The final breakdown of purines (uric acid, allantoin,
alantoic acid). Catabolism of pyrimidine bases. The final decay of pyrimidines (beta-
alanine, beta-amino isobutyric acid, NH3, CO2).
Biosynthesis of NA. Biosynthesis of purine and pyrimidine nucleotides.
Biosynthesis of polynucleotides of DNA and RNA.
Ways of synthesis of nucleotides (“saving” way and de novo way). Synthesis of
purine nucleotides, for example, IMP (sequence of reactions). Synthesis of purine
nucleotides (ATP and GTP). Pharmacotherapy: inhibitors of purine synthesis. De Novo
synthesis of pyrimidine. Synthesis of pyrimidine nucleotides (UTP and CTP).
Pharmacotherapy: inhibitors of pyrimidine synthesis. Synthesis of deoxynucletides. De
Novo synthesis of nucleotides. Formation of trinucleotides, polynucleotides of RNA,
DNA. Coding of genetic information. DNA replication (replicating “fork”, stages, and
enzymes).
Transcription is the synthesis of RNA (stages: initiation, elongation, termination,
inhibitors of transcription). Reverse transcription. The life cycle of a retrovirus.
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Thematic Module 6. Metabolism and its reflection in the biochemical parameters
Theme of lecture lesson 1. Metabolism and its characteristics by biochemical
parametrs of urine
Biochemistry of urine. The production of urine. ‘Thresholds’ and non ‘thresholds’
substances of primary urine. Final urine volume (normal, polyuria, oliguria, and anuria).
The chemical composition of urine. The composition of urine in normal and
pathological conditions (pH, cations, and anions of urine).
Examples: indicators of urine in normal and pathological states. Organic
components of normal urine: urea, uric acid, creatinine, and creatine, hippuric acid,
indican, amino acids (hyper-amino aciduria), lactic and pyruvic acid, as well as
phosphates, NH3, glucose, ketone bodies.
Theme of lecture lesson 2. Biochemistry of products of animal origin
Biochemistry of milk. Pathological processes during lactation of animals.
pH and chemical composition of milk. Electrophoretic composition of milk
caseins. Carbohydrates in milk. Lactose intolerance. Butterfat.
Biochemistry of muscle tissue, eggs, skin and wool. Norm and pathology. Study
and control of metabolism, connection with appropriate nutritional conditions.
Biochemistry of honey. Features of honey formation. Chemical composition and
biochemical properties of honey. Biochemical processes in bee honey during storage.
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The structure of the discipline
Titles of thematic
module and themes
Hours
Full-time Extramural study form
total including total including
L P Labv Ind self L P Labv Ind self
1 2 1 2 1 2 1 2 1 2 1 2 1
Thematic Module 1. Fundamentals of Physical and Colloidal Chemistry
Theme 1. Biochemistry
of Animals is the
history of its
development and its
place among the natural
sciences.
6 2 2 2
Theme 2. Fundamentals
of Physical Chemistry 12 6 6
Theme 3. Fundamentals
of Colloidal Chemistry 12 4 4 4
Total for the thematic
module 1 30 12 12 6
Thematic Module 2. Physico-chemical methods of research in biochemistry
Theme 1. Physico-
chemical methods of
research in biochemistry
30 4 6 20
Total for the thematic
module 2 30 4 6 20
Thematic Module 3. Biochemistry: Statics
Theme 1. Cell and its
organic compounds.
Carbohydrates
8 4 4
Theme 2. Lipids and
biomembranes 8 2 2 4
Theme 3. Amino acids,
peptides, proteins, 8 6 2
Theme 4. Nucleosides,
nucleotides and nucleic
acids
6 2 4
Total for the thematic
module 3 30 14 12 4
Thematic Module 4. Regulatory effects of inorganic and organic substances on the metabolism
Theme 1. Biological
membranes. Water and
minerals in animals and
plants, biochemistry of
transmembrane transfers
of minerals and organic
substances.
7 2 4 - 1
Theme 2. Vitamins.
Coenzymes 7 2 4 - 1
Theme 3. Enzymes and
their kinetic properties 7 2 4 - 1
Theme 4. Hormones 7 2 4 - 1
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and mechanisms of their
influence on metabolic
processes
Total for the thematic
module 4 28 8 16 - 4
Thematic Module 5. Dynamic and Functional Biochemistry
Theme 1. Biochemistry
of digestion and features
of digestive processes in
different organisms
5 2 2 1
Theme 2. Carbohydrate
metabolism and its
features in different
species of animals
13 4 8 1
Theme 3. Amphibolic
transformation of
organic substances
(TCAC). Energy of
biochemical processes
7 2 4 1
Theme 4. Metabolism
of lipids 5 4 2 1
Theme 5. The metabolic
processes of proteins
and some amino acids
9 4 4 1
Theme 6. Catabolism
and anabolism of
nucleotides and nucleic
acids
7 2 4 1
Total for the thematic
module 5 48 18 24 6
Thematic Module 6. Metabolism and its reflection in the biochemical parameters
Theme 1. Some
biochemical parameters
of biological fluids as a
reflection of the state of
metabolism in the
organism
7 2 2 3
Theme 2. Biochemistry
of products of animal
origin
7 2 3 2
Total for the thematic
module 6 14 4 5 5
Course project (work)
__________________
__________________
(if it is in the working
educational plan)
- - - -
Total hours 180 60 75 45
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3. Themes of seminars (not planned)
# Name of theme Hours
1
2
...
4. Themes of practical classes (not planned)
# Name of theme Hours
1
2
...
1. Themes of laboratory studies # Name of theme of laboratory studies M 1- M-3 Hours
1-2 M-1. Rules of lab-work and safety in biochemical lab. Facilities, table
wires, solutions and reagents of biochemical laboratory.
Fundamentals of Physical and Colloidal Chemistry
Solutions. рН. Methods of pH determination: indicator and ionometric.
Determination of pH in the biological samples 4
The buffered solution. Preparation of the acetate and phosphate buffers
and calculation their pH. Determination of buffer capacity.
Determination of influence of dilution on the buffered solution pH and
capacity. 3-4 Osmosis. Osmotic pressure in biological systems. The effect of
solutions with different osmotic pressure on cells. Osmotic pressure in
the erythrocytes. Fenomenon of the blood hemolysis caused by
changes of osmotic pressure. 4
Sorption and biological fenomena. Adsorbtional ability of such
sorbents as electrolytes, dyes and sols. Adsorptional ability of coal.
The processes of sorption and desorption. Fuxin adsorption on glass
and its desorption. 5-6 Colloidal solutions. The high molecular substances in biological
fluids. Preparation of colloidal solutions using dispersion. Preparation
of Fe(OH)3 by method of hydrolysis. Preparation of sol of “Berlin
blue”. Preparation of sol of silver. Peculiarities of colloidal solutions.
Determination of charge (+ or -) of particles. Coagulation of colloidal
solutions. Study of colloidal protection. Irreversible coagulation of
organic colloids
4
Thematic Module 1.
Fundamentals of Physical and Colloidal Chemistry
7-8 M-2 Physico-chemical methods of research in biochemistry
Spectophotometric and Colourmetric methods.
Calibration graf building in the purpose of protein concentration
determination with “biuret” reagent.
Centrifugation. Preparation of glycogen from animal tissues by
methods of Pfluger. Cell fractionation by centrifugation (model-
experiment)
Fundamentals of electrophoretic separation of high molecular
substances. Determination of protein fractions of blood serum by
electrophoresis. Determination of protein fractions of blood serum by
4
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turbid-dimetric method. 9-10 Methods of Chromatography. Calculation of Rf of lipid fractions in
muscles for experimental results of some studies by thin layer
chromatography. Separation of amino acids (or dyes) mixture by the
method of paper chromatography.
Thematic Module 2.
Physico-chemical methods of research in biochemistry
4
M-3. Biochemistry: Statics
Carbohydrates: colour tests on starch and glycogen. Colloidal
peculiarities of starch. Acidic hydrolysis of starch. Cellulose dissolving
in ammoniac solution of copper oxide (reagent of Shvaytzer).
Carbohydrates: mono-, disaccharides. Identification of OH-groups in
monosaccharaides. Reactions of oxidation of carbohydrates with
aldehyde-group and reduction of metal ions in basic solution (Test of
Trommer). Quantative determination of glucose in solution by Felling
method. Selivanov test on ketohexose. Sucrose tests. Reduction of
metal ions. Sucrose colour tests. 11-12 Lipids and their components. Fat identification. Acroleine test.
Solubility of fats in different solvents. Formation of soap that is
insoluble in water. Saponification of soap. In the fats, identification of
unsaturated fatty acids (FA). Oxidation of unsaturated fats.
4 Amino acids. Example of demonstration of amino acids separation by
chromatography. Qualitative tests on amino acids: xantoprotein
reaction on amino acids; tryptophan test (reaction of Adamcevich);
reaction on sulfur containing amino acids (reaction of Foley).
Destruction of amino acids by nitrous acid. 13-14 Amides of acids. Urea and its peculiarities: preparation nitrate-acidic
salt of urea; distruction of urea at heating; biurett reaction.
Proteins. Biuret reaction. Reversible reaction of protein sedimentation
by ammonium sulfate and by alcohol. Irreversible reaction of protein
sedimentation by salts of heavy metals, by reagents to alkaloids
(tannin, potassium hexocianoferrat and picric acid), by concentrate
inorganic acids, by organic acids and by boiling. Physical and
Chemical peculiarities of proteins: determination of isoelectric point
(pI) of protein (gelatin).
4
15 Nucleic acids and their components. Isolation of
deoxyribonucleoprotein. Hydrolysis of nucleoprotein. DNA
identification in deoxyribonucleoprotein. Pentose identification.
Purines identification. Phosphoric acid determination in hydrolysates.
2
Thematic Module 3. Biochemistry: Statics
Total hours 30
№
з/п Name of theme of laboratory studies М 4-6 Hours
1. M-4. Regulatory effects of inorganic and organic substances on the
metabolism
Role of mineral substances in the metabolic processes.
The role of macro- and microelements in metabolism. Determination of
trace element (Fe) and macronutrients (Mg, Cl) and using different
methods in biological samples.
4
2. Some representatives of vitamins. Coenzymes.
Fat-soluble vitamins, their detection and role. Qualitative reactions to
vitamins A (samples with ferric chloride and sulfuric acid), E (sample with
4
16
nitric acid).
Water-soluble vitamins, their role as coenzymes. Qualitative reactions to
vitamins: B1, B2, B5, and C. Quantitative determination of vitamins C and
riboflavin (vitamin B2) in biological samples
3. Enzymes. Kinetic aspects
Effect of temperature and pH on the activity of amylase. Specificity of
enzymes (amylase). Determination of amylase activity. Effect of activators
and inhibitors on enzyme activity. Kinetic properties of amylase.
4
4. The role of hormones in metabolic processes
Qualitative reactions to hormones. Qualitative reactions to adrenaline: tests
with iodine and iron (III) chloride. Qualitative reactions to insulin: biuret
reaction to insulin; reactions to sulfur-containing amino acids. Quantitative
determination of adrenaline by colorimetric method.
4
5 Thematic Module 4. Regulatory effects of inorganic and organic substances
on the metabolism.
2
6. M-5. Dynamic and functional biochemistry
Carbohydrate metabolism, its intermediates
Investigation of the properties of mono- and disaccharides. Quantitative
determination of glucose in a biosample by the Fehling method. Reaction to
disaccharides. Barfed's reaction.
Investigation of the properties of polysaccharides. Detection of glycogen in
the liver. Isolation of glycogen by the Pfluger method. Glycogen
hydrolysis. Determination of glycogen content in tissues.
Control work: glycolysis, glycogenolysis, fermentation, pentose phosphate
cycle
8
7 Biological oxidation of substances and their energy metabolism
Quantitative determination of lactic acid in the serum of animals by
colorimetric method and its detection in muscles; determination of muscle
adenosine triphosphatase activity.
Control work: TCAC, biological oxidation
4
8 Lipid metabolism and its intermediates
Detection of fats. Acrolein test. Determination of iodine and acid number
of fat. Qualitative reaction to bile acids.
Control work: β-oxidation of FA
2
9 Protein metabolism intermediates and their characteristics (I)
Influence of temperature and reaction of the environment on the solubility
of proteins. Physico-chemical properties of proteins. Determination of the
isoelectric point of a protein (casein). Protein precipitation reactions
(organic acids: trichloroacetic, picric; organic solvents: alcohol, acetone).
Quantitative determination of protein by the Lowry method.
Control work: transformation of amino acids
2
10 Protein metabolism intermediates and their characteristics (II)
Qualitative reactions to aromatic amino acids. Reaction to phenylalanine,
tyrosine, and tryptophan. Reaction to tyrosine. Reaction to tryptophan.
Reaction to thioamino acids.
Control work: synthesis of urea
2
11 Nucleic acid metabolism intermediates.
Isolation of nucleoproteins from the liver of animals and study of their
chemical composition
Detection of DNA in deoxyribonucleoprotein. Qualitative reaction to the
presence of phosphoric acid
Control work: synthesis of uric acid
2
12 Thematic Module 5. Dynamic and Functional Biochemistry 2
17
13 M-6. Metabolism and its reflection in biochemical parameters
Biochemical parameters of biological fluids
Determination of inorganic components of urine (determination of
chlorides, sulfates, phosphates). Determination of pathological components
of urine (samples for protein, sugar, pigments, acetone bodies).
2
14 Biochemistry of products of animal origin Obtaining whey of milk. Precipitation and isolation of casein. Determination of
milk acidity. 1
15 Thematic Module 6. Metabolism and its reflection in biochemical
parameters 2
Total hours 45
18
Test question, the tests sets to determine the level assimilation of knowledge by
students.
Part 1
Biochemistry (common):
1. Metabolic processes of microorganisms in rumen and their influence on living
ability of cows are one of the subject of study … (of what biochemistry)
2. Static biochemistry does study...
3. Dynamic biochemistry does study...
4. Functional biochemistry does study...
5. Who got Nobel Prize for discovery of cytric acid cycle or tricarboxylic acids
cycle in 1953?
6. The indicated below substances are belong to …
7. It’s necessary to choose right definition of process presented on picture below...
Fundamentals of Physical and Colloidal Chemistry:
8. How many grams of Calcium Chloride (CaCl2) and water is necessary for
preparing 150 g with mass fraction of Calcium Chloride 3%
9. How many grams of Potassium Chloride (KCl) and water is necessary for
preparing 280 g with mass fraction of 5 % KCl?
10. How many grams of lactose (С12Н24О12) and water is necessary for preparing 300
g with mass fraction of lactose 7 %?
11. How many grams of glucose (С6Н12О6) and water is necessary for preparing 100
g with mass fraction of glucose 10 %?
12. What solution is isotonic? Solution is isotonic when …
13. What solution is hypotonic? Solution is hypotonic…
14. What solution is hypertonic? Solution is hypertonic…
15. What index is measured with pH-meter?
16. What value of pH of human blood?
17. What acidosis is? Acidosis is …
18. Mechanism of protein buffer system effect is based on …
19. Protein buffer system is mainly consisted of...
20. What is the 1st law of Raul about?
21. What is the 2nd law of Raul about?
22. What process is called absorption?
23. What process is called adsorption? Adsorption is called …
24. How is sole distinguished from true solution?
25. What protective colloid has the greatest power?
26. Please, choose the right phrase about protective power of some colloids
Methods:
27. Spectral characteristics of nucleoside are determined with what device?
28. What is possibility of centrifugation? Please, give characteristic of the method.
19
29. In medico-biological investigation, what is used in the purpose to separate
biopolymers, viruses and subcellular elements?
30. General description of electrophoretic method.
31. What is possibility of electrophoresis? Please, give characteristic of the method.
32. What is possibility of gel-filtration?
33. Common characteristics of ion-exchanged chromatography.
34. Common characteristics paper chromatography.
Carbohydrates:
35. What is monomer of polysaccharide?
36. Monomer(s) of maltose is/are …
37. Monomer of isomaltose is/are …
38. Monomer(s) of succrose is/are …
39. Monomer(s) of lactose is/are …
40. Monomer(s) of cellobiose is/are …
41. Monomer(s) of tregalose is/are …
42. After fermentation, the disaccharide (see below) is hydrolyzed into two
monomers. It’s necessary to choose right equation of disaccharide hydrolysis.
43. Monomer(s) of starch is/are …
44. What significance/role of starch is?
45. Monomer(s) of glycogen is/ are …
46. What significance/role of glycogen is?
47. Monomer(s) of cellulose is / are…
48. What significance/role of cellulose is?
49. It’s necessary to choose polysaccharide which has mainly monomer fructose
50. It’s necessary to choose polysaccharide which is accumulated as carbohydrate
storage in wheat seeds
51. Polysaccharides - levan and flein, are belonged to …
52. What significance/role of polysaccharides are?
53. Monomer of mannan-polysaccharides is…
Lipids:
54. What saturated fatty acids do you know?
55. What significance/role of saturated acids is?
56. What unsaturated fatty acids do you know?
57. What significance/role of unsaturated acids is?
58. What organic substance does glycerol belong to?
59. What significance/role of glycerol is?
60. What organic substance does cholesterol belong to?
61. What significance/role of cholesterol is?
62. What organic substance does sphyngosine belong to?
63. What significance/role of sphyngosine is?
64. What organic substance does ethanol belong to?
65. What organic substance does wax belong to?
66. What significance/role of wax is?
67. Stearic acid is saturated carboxylic acid or not?
20
68. Oleic acid is saturated carboxylic acid or not?
69. Tristearoil glycerol is composed of …
70. Monogalactosyl diacyl glycerol is composed of remains of …
71. Cholesteride is …
72. The glycerol presence can be discovered by ‘akrolein’-test. What substances
would have positive ‘akrolein’-test?
73. Phosphatidyl ethanol amine is composed of …
74. Sphingophospholipids are …
75. What significance/role of sphingolipids are?
Proteins:
76. Structural organization of protein (common characteristics)
77. What is monomer of protein?
78. Primary structure of protein (common characteristics)
79. Secondary structure of protein (common characteristics)
80. Tertiary structure of protein (common characteristics)
81. Biosynthesis of protein (common characteristics).
82. The first spatial structure of hemoglobin and myoglobin were determined with X-
ray analysis by scientists who got Nobel Prize. These scientists are John Kendrew
and …
83. It’s necessary to choose the conjugated protein containing hem:
84. It’s necessary to choose the conjugated protein containing Cu?
85. It’s necessary to choose the conjugated protein containing transferrin and ferritin?
86. It’s necessary to choose the conjugated protein containing casein?
87. Casein and pepsin are belonged to what conjugated proteins?
88. What significance/role of casein is?
89. What significance/role of pepsin is?
90. In what set of amino acids are all of them belonged to monoamino
monocarboxylic acids?
91. What amino acids are essential?
92. What significance/role of essential amino acids are?
93. Does phenylalanine be essential amino acid?
94. Does tryptophan be essential amino acid?
95. Does tyrosine be essential amino acid?
96. Does lysine be essential amino acid?
97. Does methionine be essential amino acid?
98. Does glycine be essential amino acid?
99. Does alanine be essential amino acid?
100. Does serine be essential amino acid?
Nucleic Acids:
101. What is monomer of nucleic acid?
102. What purine nucleobases do you know?
103. What pyrimidine nucleobases do you know?
104. Structural organization of nucleic acid
105. Primary structure of nucleic acid (common characteristics)
21
106. Secondary structure of nucleic acid (common characteristics)
107. Tertiary structure of nucleic acid (common characteristics)
108. Please, make a row of main events in some transformation according to
central dogma of molecular biology.
109. What difference between DNA and RNA?
110. What fuctions of DNA do you kow?
111. What fuctions of RNA do you kow?
112. What fuctions of mRNA do you kow?
113. What fuctions of tRNA do you kow?
114. What fuctions of rRNA do you kow?
115. Synthesis of ribonucleic acid (common characteristics)
116. Synthesis of deoxyribonucleic acid (common characteristics)
117. Who did formulation of rule of complementation between purine and
pyrimidine bases in DNA?
118. Please, indicate a right pair of nucleoside and nucleobase (nucleoside –
Nitrogen containing base is corresponded with this nucleoside):
119. According to the principle of complementarities, it’s necessary to calculate
the molar content of uracil in DNA when there are 158 mol of adenine.
120. Replication of DNA sequence of GGTTGCCAA results …
121. What common characteristics of replication are?
122. According to the principle of complementarities, it’s necessary to calculate
the molar content of thymine in DNA when there are 632 mol of adenine.
22
Part 2
1. Formation of ethanol amine (in the activated form)
2. Build right chain of reactions of the urea cycle from citrulline
3. Build right chain of reactions of the urea cycle from urea
4. Build right chain of reactions of the urea cycle from arginine
5. Build right chain of reactions of the urea cycle from ornithine
6. What class of vitamins do the substances belong to?
7. How does somatotropin influence gluconeogenesis in the liver?
8. Functional biochemistry does study...
9. Glycerol oxidation: glycerol phosphokinase reaction (it’s necessary to choose substrates
and products).
10. What peculiarities of baby-digestions (it’s about enzymes in the different compartments of
digestion-tract?
11 It’s necessary to write names of substrates, products and enzyme of the reaction
represented below (You can make this task if you know: what pathway is represented
by one reaction here).
12 Under transamination of pyruvate, it is formed such important substrate of
gluconeogenesis as ...
13 Distraction of phospholipids: it’s necessary to give characteristic of reaction that
catalyze by phospholipase D (substrates, products).
14 How it could be lowered the glucose level in the dog’s blood (under conditions of
diabetus mellitus)?
15 Lactic acid fermentation: under fermentation by Bact. lactis, lactic acid is formed from
glucose: C6H12O6 -> 2 CH3-CHOH-COOH;
16. ... is compartment of such enzymes as carboanhydrase, uricase, urease, aldolase, and
phosphatase.
17. What enzyme does digestion of proteins?
18. Glyceraldehyde-3-phosphate dehydrogenase reaction of glycolysis:
19. (NAD-dependent) isocitric acid reaction of TCAC:
23
20. Enzymes can be consisted of what class of organic substances? Enzymes can be
consisted o f . . .
21. What function do biological membranes in animal organism?
22. ‘Philohinon’ and ‘pharnohinon’ are natural forms of vitamin ...
23. What is modification of the ‘key-lock’model which is characterized enzymatic action?
24. What enzymes do hydrolysis of the nucleic acids component of nucleoproteins?
25. Who was the first scientist that showed importance of vitamins?
26. Role of water-soluble vitamins, especially vitamin P:
27. What reaction is catalyzed by hydrolases?
28. What enzymes do ‘digestion’ of lipids?
29. What coenzyme takes part in the reaction of formylation and formation of methyl-
groups?
30. What element takes part in the process of oxidative phosphorylation?
31. It’s necessary to choose a name of biological active substance which is catalyzed by
chemical processes in the organism
32. It’s necessary to choose substrates and products of the carbamoyl phosphate synthase
reaction of the urea cycle (substrates, products)
33. What is the second irreversible reaction of glycolysis (according to the name of
enzyme)?
34. Formation of choline (in the activated form):
35. Build right chain of reactions of the TCAC starting from a-ketoglutarate:
36. Build right chain of reactions of the TCAC starting from succinate
37. Build right chain of reactions of the TCAC starting from succinyl-CoA
38. Build right chain of reactions of the TCAC starting from fumarate
39. Build right chain of reactions of the TCAC starting from malate
40. Build right chain of reactions of the TCAC starting from oxaloacetate
41. Build right chain of reactions of the TCAC starting from citrate
42. Build right chain of reactions of the TCAC starting from isocitrate
43. All pointed out carboxylic acids belong to …
44. Cortisol (which is belonged to glucocorticoids) ... gluconeogenesis.
45. Static biochemistry does study...
46. What peculiarities of digestions in ‘mature’ animals (it’s about enzymes in the different
compartments of digestion-tract)?
47. It is necessary to choose names of substrates, products and enzyme of the reaction
represented below (You can make this task if you know: what pathway is represented by
one reaction here; substrates, products, enzyme, coenzyme).
48. Synthesis of TAG. It’s necessary to choose right reaction of glycerol-3-phosphate
formation by glycerol phosphokinase (substrate, products).
49. Catabolism of the sterol esters by enzymes (It’s necessary to choose typical reaction with
the pointed out substrates, products and enzyme).
50. Substrate phosphorylation in the TCAC is carried at step of transformation o f . . .
51. Alcoholic fermentation and its brief characteristics.
52. Role of Sodium in the animal life:
53. Glycolysis. It’s necessary to choose names of substrates and products of the reaction
catalyzed by ‘phosphoglycerate kinase’
54. The reaction of the TCAC is catalyzed by multi-enzyme complex of α-ketoglutarate
dehydrogenase (substrates and products):
55. Biological role of vitamins.
56. Biological role of fat-soluble vitamins.
57. Biological role of water-soluble vitamins.
58. Biological role of vitamin A.
59. Biological role of vitamin E.
60. Biological role of vitamin K.
61. Biological role of vitamin D.
62. Biological role of vitamin Bl.
63. Biological role of vitamin B12.
64. Biological role of vitamin B5.
65. Biological role of vitamin C.
66. Formation of histamine is ...
67. What enzymes do digestions of polysaccharides?
2
68. What microelement is in a structure of hemoglobin, or myoglobin, or cytochromes?
69. Role of water-soluble vitamins, especially C.
70. How does enzyme work concerning the energy reaction activation (Ea)?
71. What enzymes do digestion of lipids?
72. Role of Nitrogen in the animal life:
73. The substances as ... belong to vitamin F.
74. What reaction does catalyze by lyase?
75. What enzymes do digestion of carbohydrates?
76. Who showed the enzyme activity dependence of pH of medium?
77. Enzymes of protein synthesis are localized mostly in ...
78. Zinc is belonged to ...
79. Biosynthesis of urea is in the...
80. What is the third irreversible reaction of glycolysis (according to the name of enzyme)?
81 Phosphoglycerate mutase reaction of glycolysis (at the end of the tests)
82 Build a chain of chemical transformations in the glycolysis starting from hexose
83 In the table, enzymes take part in the processes of...
84. The ... biochemistry does study the transformation of substances up to the end-
products of metabolism
85. β-oxidation of fatty acids: what is going on in reaction catalized by carnithine
acyltransferase I?
86. In the humane organism, it’s founded Cu-deficit that causes lowering enzyme activity
o f . . .
87. Role of choleic acid in digestion of lipids:
88. Role of fat-soluble vitamins, especially vitamin F.
89. Localisation of processes of β-oxidation (activation of FA and actually their β-oxidation):
90. Alcali reserve of blood mainly is ...
91. Glycerol oxidation: glycerolphosphokinase reaction (it’s necessary to choose substrates
and products).
92. What peculiarities of baby-digestions do you know (it’s about enzymes in the different
compartments of digestion-tract)?
3
93. It’s necessary to write names of substrates, products and enzyme of the reaction
represented below (You can make this task if you know: what pathway is represented by
one reaction here).
94. Under transamination of pyruvate, it is formed such important substrate of
gluconeogenesis as ...
95. Distraction of phospholipids: it’s necessary to give characteristic of reaction that
catalize by phospholipase D (substrates, products).
96. How it could be lowered the glucose level in the dog’s blood (under conditions of
diabetus melitus)?
97. Lactic acid fermentation: under fermentation by Bact. lactis, lactic acid is formed from
glucose: C6H,206 2 CH3-CHOH-COOH;
98 … is compartment of such enzymes as carboanhydrase, uricase, urease, aldolase, and
phosphatase.
99. What enzyme does digestion of proteins?
100. Glyceraldehyde-3-phosphate dehydrogenase reaction of glycolysis:
101. (NAD-dependent) isocitric acid reaction of TCAC:
102. Enzymes can be consisted of what class of organic substances? Enzymes can be
consisted of...
103. Role of Selenium in the animal life:
104. What is biological importance of glucose-lactate cycle?
105. What is biological importance of the pentose phosphate pathway fuctioning in the
erythrocytes?
106. Role of Ferum in the animal life:
107. The reaction of the TCAC is catalized by succinyl thiokinase (substrates and
products):
108. Carotenoids are precursors of ... vitamin
109. What is remarkable characteristic of urease?
110. What enzymes do digestion of oligosaccharides?
111. What disease progresses under conditions of Iodine deficit in diet?
112. What class of enzyme does El belong to (according Enzyme Classification)?
4
113. What name of substances are under “3” in the scheme of synthesis of uric acid?
114. What enzymes do digestion of phospholipids?
115. What is “a main purpose” of ornithine cycle?
116. Under transamination of oxaloacetate, it is formed such important substrate of
gluconeogenesis as ...
117. What reaction is catalyzed by isomerase?
118. What enzymes do digestion of proteins?
119. Enzymes of cellular respiration are mainly localized in ...
120. Butyric acid fermentation:
121. Sodium exchange is regulated by ...
122. Ornithine transcarbomoyl transferase reaction of the urea cycle (substrate and
products)
123. Increase secretion of adrenaline leads to ... glucose level in the blood
5
National University of Life and Environmental Sciences of Ukraine
ED «Master»
Training direction
Veterinary Medicine
Department of
Biochemistry
and Physiology
of Animals
20__-20__
Tests form № _1_
of Discipline
Biochemistry of Animals with
Fundamentals of Physical and
Colloid Chemistry
"CONFIRM"
Head of Department
________________
(signature)
Tomchuk V.A.._( Family name, initials)
____________20___ р.
Test questions
(the maximum score is 10 points for every question)
1. What is possibility of electrophoresis? Please, give characteristic of the method.
2. According to the principle of complementarities, it’s necessary to calculate the molar content of uracil in DNA when there are 158
mol of adenine. If it’s impossible, you can give right name of nuclear base for such calculation.
Test tasks of various types
(the maximum score is 10 points for every question)
1. Monomer of tregalose is …
2. Metabolic processes of microorganisms in rumen and their influence on living ability of cows are one of the subject of study …
A) Ecological Biochemistry;
B) Biochemistry of microorganisms;
C) Biochemistry of Animals;
D) Plant Biochemistry;
E) Evolutional Biochemistry. 3. How many grams of Potassium Chloride (KCl) and water is necessary for preparing 280 g with mass fraction of 5 % KCl?
A 5 g, 275 g D 14 g, 266 g
B 28 g, 152 g E 20 g, 260 g
C 10 g, 270 g
4. Please, indicate a right pair (nucleoside – Nitrogen containing base is corresponded with this nucleoside):
A Adenine-adenosine C Uridine- uracil D Thymine-thymosine
B Guanosine-adenine E Thymidine-uracil
5. What amino acids are essential?
A) phenylalanine, tryptophan, tyrosine;
B) lysine, phenylalanine, tryptophan;
C) methionine, phenylalanine, glycine;
D) glycine, phenylalanine, tryptophan;
E) alanine, phenylalanine, tryptophan
6. It’s necessary to choose the conjugated protein containing hem:
A chylomicrons D ferritin
B immunoglobulin G E myoglobin
C ribosome
7. Monogalactosyl diacyl glycerol is composed of remains of …
A) glycerol, 2 fatty acids, glucose;
B) glycerol, 2 fatty acids, lactose;
C) glycerol, 2 fatty acids, galactose;
D) glycerol, 2 fatty acids, fructose;
E) glycerol, 2 fatty acids, galactourose.
8. Cholesteride is …
A) ester of high molecular monoatomic alcohols and high molecular FA ;
B) ester of miricilic alcohol and high molecular FA ;
C) ester of glycerol and 3 high molecular FA ;
D) phosphoric esters of ceramides and amino alcohols: choline, ethanol amine and serine ;
E) ester of cholesterol and high molecular FA.
9. How is sole distinguished from true solution?
A) Tyndall effect is specific for a true solution;
B) Tyndall effect is specific for a colloidal solution;
C) Tyndall effect is specific for molecular-ionic solutions;
D) Tyndall effect is specific for colloidal and molecular-ionic solutions;
E) Tyndall effect can be used to distinguish a molecular-ionic solution from a pure
liquid.
10. The glycerol presence can be discovered by ‘akrolein’-test. What substances would have positive ‘akrolein’-test?
A) bovine fat & spermaceti
B) fish fat & oleic acid
C) sunflower oil & bee wax
D) wax & mineral oil
E) bovine fat & sunflower oil
6
National University of Life and Environmental Sciences of Ukraine
ED Master
Direction of training
Veterinary Medicine
Department of
Biochemistry and
Phisiology of Animals,
20__-20__ educational.
year
EXAM TEST № _1_
of discipline
Biochemistry of Animals
with the Fundamentals of
Fhysical and Colloid
Chemistry
Confirm
Acting as Heads
________________
(signature)
Tomchuk V.А._(Fn,Init)
____________20___
Examination questions
(The maximum score is 10 points for every question)
1. What participants of TCAC reaction precede the formation of malate?
2. Create a series of changes to the ribosome during protein biosynthesis, where the last step was the formation
of peptide bond
Tests of various types
(The maximum score is 10 points for answers to tests)
1 Below pointed compounds can be called ..
…
AMP ADP ATP CMP GMP GDP
UDP UMP UTP CDP CTP GGP
(in the form of answers write in short)
2. Synthesis of TAG: Describe diacylgycerol-acyltransferase reaction (substrates, products).
A) phosphatidic acid → 1,2-diacyl glycerol + Pi
B) dyoxyacetonphosphate + NADH + + H + → glycerol-3-phosphate + NAD +
C) phosphatidic acid + acyl-CoA → 1,2-diaсyl glycerol + CoASH
D) glycerol-2-phosphate → glycerol-3-phosphate
E) 1,2 diacylglycerol + acyl-CoA → triacyl glycerol + CoASH
3. . The first stage of pentose phosphate pathway is called ...
4. How are monoacyl glycerols absorbed?
A) monoacyl glycerols are absorbed by simple diffusion;
B) monoacyl glycerols are absorbed by pinocytosis;
C) monoacyl glycerols are absorbed by simple diffusion or pinocytosis;
D) monoacyl glycerols are absorbed in combination with bile acids;
E) monoacyl glycerols are absorbed by phagocytosis;
5. What are 3 reactions in glycolysis irreversible?
A) mutase, phosphofructokinase, pyruvate kinase reactions
B) hexokinase, phosphofructokinase, pyruvate kinase reactions
C) hexokinase, phosphofructokinase, lactate dehydrogenase reactions
D) hexokinase, aldolase, pyruvate kinase reactions
E) triosophosphate isomerase, aldolase, enolase reactions
6. What level of the Pentose Phosphate Pathway function effectiveness is in the tissues with a predominance of
oxidative metabolism (for example, sceleton muscles)?
A) high level;
B) low level;
C) stable low level; D) the depressed level;
E) no changes
7. Glucokinase reaction of glycolysis.
A) substrate: phosphoenol pyruvate, ADP, H2O; product - pyruvate, ATP
B) substrates: glyceraldehyde-3-phosphate, Pi, NAD +; products - 1.3 diphosphoglycerate, NADH (H+);
C) substrates: 1.3 diphosphoglycerate, ADP, NAD+; products - 3-phosphoglycerate, ATP;
D) substrate: glucose, ATP; product - glucose-6-phosphate, ADP;
E) substrate: 2-phosphoglycerate, H2O; product - phosphoenol pyruvate
8. Fumarate hydratase (fumarase) of TCAC reaction has …
A) substrates: isocitrate, NAD+; products: α-ketoglutarate, NADH (H+), CO2;
B) substrates: succinate, FAD; products - fumarate (trans-compound) FADH2;
C) substrates: acetyl-CoA, oxaloacetate, H2O; products - citrate, CoA-SH;
D) substrates: isocitrate, NAD+; Products: alpha-ketoglutarate, NADH (H+);
E) substrates: fumarate, H2O; Product: Malate;
9. What enzymes do digestion of carbohydrates?
A) protease, trypsin, pepsin, transferase;
B) phosphodiesterase, nukleozidase, ligase
C) lipase, phospholipase, holesterol esterase
D) amylase, succrase, maltase, celobiase
E) nuclease, lipase, amylase
10. Microelement (that has antioxidant properties) is involved in oxidative phosphorylation, along with vitamins
E and produces radioprotective effect, and there is:
A) Zn B) Co C) Mo D) Mn E) Se
7
Methods of teaching
Methods of teaching (methods (greek) - ‘a way of knowing the way of finding
the truth’) - the streamlined ways of the interrelated, purposeful activity of the teacher
and students for the effective resolution of problems of study discipline "Biochemistry
of Animals with Fundamentals of Physical and Colloidal Chemistry". Methods of
teaching are implemented via the system of instruction (actions of teacher and students,
implemented the requirements of various methods) and of training activities (various
training equipment used in the system of cognitive activity: books, laboratory
equipment, facilities).
Below are teaching methods used on core classroom training sessions of
discipline "Biochemistry of Animals with Fundamentals of Physical and Colloidal
Chemistry" and during independent work of students.
By source and nature of the transmission of information perception, generally,
there are three groups of teaching methods:
• verbal (narrative, explanation): the story is a method of study involving
narrative, a descriptive form of disclosing educational material (involving
imagination of student); explanation is the verbal learning method (whereby the
teacher reveals the essence of a phenomenon, the law of the process), based on
logical thinking with prior experience of students;
• visual (demonstration, illustration): demonstration is a method of teaching
which involves showing objects and processes actually in dynamics; illustration
is a method of teaching in which objects and processes are revealed through their
symbolic images (photographs, drawings, charts, graphs etc.)
• practical (laboratory method, practical work, exercise, observation): laboratory
method involves the organization of training activities through the use of special
equipment and specific technologies for acquiring new knowledge or test
scientific hypotheses at the level of research; practical work aims to use the
knowledge gained in the resolution of practical tasks (for example, performing
some kind of experiment or its fragment in biochemical research of scientists);
exercise is a method of teaching, the essence of which is to deliberate, repetition
by students some actions or operations to the formation of skills (for example,
ability to use machinery and equipment of biochemical laboratory); observation
as a method of training involves perception of certain objects, phenomena and
processes in natural and laboratory environment without interfering with these
phenomena and processes.
Studying the structure, physico-chemical and biological properties of natural
compounds, their metabolism, regulation and correction of metabolic processes by
exogenous and endogenous factors used the teaching methods that are different in
character logic of knowledge, namely:
8
- analytical method that involves thinking or practice schedules whole into parts in
order to study their essential features;
- inductive method, which is the way of examining objects, events from the unit to
the total;
- deductive method, based on a study of educational material from general to
specific, single;
- ‘traduktyvnyy’ method that provides findings from individual to individual, and
the particular to the particular, from the general to the general.
The above methods are used on core classroom training sessions of (see below)
subject "Biochemistry of Animals with Fundamentals of Physical and Colloidal
Chemistry".
The main types of lessons of discipline "Biochemistry of Animals with
Fundamentals of Physical and Colloidal Chemistry" are the classes: auditorium classes
(lecture, laboratory sessions, and consultations) and independent study of students.
Educational Lecture of discipline "Biochemistry of Animals with Fundamentals
of Physical and Colloidal Chemistry" is logically verified, scientifically sound and
systematic exposition of scientific questions that cover the structure, physico-chemical
and biological properties of natural compounds, their metabolism, regulation and
correction of metabolic processes using a fodder and medicines to strengthen health and
improve animal productivity. Lecture course "Biochemistry of Animals with
Fundamentals of Physical and Colloidal Chemistry" is illustrated and presented in a
presentation (PDF-files are provided to students) to better absorption of the material.
As the lecture is one of the main types of classes and simultaneously teaching
methods in higher education, it is intended to form a basis of knowledge of students in
biochemistry of animals and fundamentals of physical and colloid chemistry, as well as
determine the direction, the main content and nature of laboratory work and
independent students' work on the subject "Biochemistry of Animals with Fundamentals
of Physical and Colloidal Chemistry".
Laboratory lesson is a type of instruction where under the guidance of the
teacher, students conduct real or model experiments or experiments in specially
equipped training labs using equipment suited for the educational process. Herefrom,
didactic purpose of laboratory studies is the practical proof of certain theoretical
positions subject "Biochemistry of Animals with Fundamentals of Physical and
Colloidal Chemistry", the acquisition of practical skills and experience working with
complex equipment, equipment, computers, instrumentation, experimental methods of
biochemical research.
Stages of preparation and conduct laboratory class are: pre-control training of
students in a particular laboratory work; specific tasks in accordance with the proposed
theme, design custom reports, assessment results of student by teacher.
It must be noted that in the case of laboratory work relating to the possible danger
9
to the health and lives of students, a mandatory step in its preparation and conduct are
instructed on safety rules and monitoring their compliance, conducted as the first lesson
(general instruction work in biochemical laboratories), and these (training on individual
possibly dangerous conditions of the experiments).
Consultation is one of the types of classes that is conducted to obtain student
responses to some theoretical or practical aspects of biochemistry animals and to clarify
certain aspects of the theoretical principles or their application in veterinary medicine.
Consultations during the semester (current consultations semester) and before control
measures (exam) held on schedule of Dean's office.
Independent work or self-work is the primary means of learning student
educational material on the biochemistry of animals at the time free from mandatory
training sessions.
In this course, an independent work or a self-work is performed as a study of the
use of methods, methodological approaches and techniques based on published research
materials in the form of books, manuals, guidelines, patents, etc. (*it’s pointed themes
of self-work in the thematic material of lectures). Methods of teaching in terms of independent mental activities:
- the problem statement, which provides for the creation by a teacher the
problematic situation, help students in the selection and "acceptance" problem task;
- partial search method that involves students in finding ways, methods and means
of resolution of cognitive tasks;
- research method that aims to include students in independent resolution of
cognitive tasks with the necessary equipment.
Forms of control
For application and by nature, control is divided into the previous, current,
periodic, final, mutual control, self-control.
Previous monitoring conducted to determine the level of preparedness of
students for the new school year or semester. The results of this control significantly
affect the initial clarification of the situation to further the educational process in higher
education, detalisation, optimization and more focused definition of its semantic
component, substantiation of sequence processing sections and parts of the course
"Biochemistry of Animals with Fundamentals of Physical and Colloidal Chemistry",
determination of basic techniques, forms and means of its implementation, etc.
Current control is used for testing as individual students, as academic groups,
usually in their daily learning activities, primarily for scheduled classes. The teacher
systematically observes students' academic work, checks the level of mastery of the
program material, the formation of practical skills and abilities, experience skills, but
also presents the corresponding estimates for oral answers, tests, practical laboratory
experiments (protocol implementation which are presented in a workbook on the subject
"Biochemistry of Animals with Fundamentals of Physical and Colloidal Chemistry",
Part 1 and Part 2), provided by the discipline.
10
Current control is educational in nature, as is aimed at stimulating students' desire
to systematically work independently of educational material, to raise their level of
knowledge and to improve the teaching skills of teachers.
Periodic monitoring (ranking with thematic modules) is a systematic, planned
and focused. It consists in determining the level and extent of mastery of knowledge,
skills and abilities late as thematic modules, and a time interval: week, month, quarter,
etc. This control is carried out in the course of routine activities (exercises), and
designated backup time.
Summative assessment (test, exam) aims to determine the level of fulfillment of
the tasks set out in the curriculum, training plan and other documents that govern the
educational process. It covers both theoretical and practical training for students, spend
it, usually at the end of the second semester (test) and third (test) as well as during
special events check.
In the educational process of the study subject "Biochemistry of Animals with
Fundamentals of Physical and Colloidal Chemistry" works in the form of mutual advice,
consultations, exchange of experience, best students help those who lag behind in
education.
Important means of control is self-control which implements the practice of the
principles of activity and consciousness, strength of knowledge, skills and abilities of
students.
There are two forms of self-control: individual and group. In case of individual
forms of control, student determines the degree of mastery of professional knowledge;
skills and abilities (most offer student objectively assesses their response). Group
provides self-assessment of their learning activities and progress achieved, as well as
the identification of weaknesses, study ways to overcome them (widely practiced in the
performance of laboratory work, exploratory theoretical work that allows students to
deepen their knowledge on a particular topic).
The main forms of test knowledge and skills, in addition to self-control, are
individual, frontal and group check.
The purpose of individual test is to determine at what level each student mastered
a complex of knowledge and skills, the development of professional skills, and to
identify major shortcomings and ways to address them.
Frontal test applied to a relatively short period of time to find out the level of
mastery of the program material. Teacher prepares particular topic short questions for
students to demand short answers to them from the place. For example, the front
paperwork.
Group test aims to determine the level of collective action, coherence and
cohesion during the tasks.
Sometimes it pays off combined test - a combination of the above forms.
According to the control objectives that define teachers to implement these types
of checks, there are used certain methods.
Methods of test are set of techniques and methods of pedagogical diagnostic
efficiency of teaching and learning of students to ensure full and meaningful
11
information about the didactic process in universities and on their effectiveness and
efficiency.
Basic methods of checking students' progress in the didactic process and
determine the effectiveness of this process:
- comprehensive monitoring,
- written works,
- oral interviews,
- practice,
- didactic tests,
- programmable control, etc.
Using the method of observation of teaching and learning activities of students
during the study subject "Biochemistry of Animals with Fundamentals of Physical and
Colloidal Chemistry", teacher knows the details of their activities (both in class and
outside of classroom time - when performing tasks of independent work attitude, will
and desire to study biochemistry, fundamentals of physical and colloidal chemistry),
finds inclinations and abilities, success, behavior, capabilities and ways of acting in
certain situations (such as when performing laboratory experiments), defines the scope
and depth of mastery of professional knowledge, the level of mastery relevant skills and
abilities, degree of formation of merit, determines shortcomings and ways to address
them more. Monitoring survey can be done at any time and for any classes.
Written control provides deep and comprehensive mastery test of program
material. With written work, there is simultaneously control of a large number of
students. This method is fairly objective, because it gives the opportunity to compare
different knowledge students using standard questions, identify theoretical knowledge,
practical skills and adequate applications for solving specific professional tasks (such as
the use of biochemistry in the practice of veterinary physician). In this analysis, the
teacher formed of each student about his strengths and weaknesses.
Objective and comprehensive analysis has a very strong educational and didactic
effect as on scientific and educational worker as on other students.
One of the testing methods is an oral survey carried out by means of interviews,
stories of student, interpretation of certain theories, ideas, opinions of professional
events and more. The biggest methodological value of oral questioning is to provide
direct live contact with the teacher learners. The basis of oral questioning is
monological answer of student or conversation. This method, due to its specificity and
the nature of the application, is used as a daily classroom routine, and the various
checks.
During the survey, special attention should be paid to the formation of benevolent
moral and psychological atmosphere in the group that interview. Initially, the teacher
clearly articulates the question, and only after a pause (15 - 20 seconds) determines the
student who has to answer. There is also practiced student to ask questions correctly,
including oral responses of other students or performances. Ability to set clear student
12
questions also indicates good possession educational material, in this case points to
deeper knowledge on relevant topics of biochemistry.
Usually, there is a higher grade deserving by students who actively offer
innovative solutions to this or that problem when studying the biochemistry of animals.
In case of failure of the student immediately give the correct answer, his thinking should
be directed in the right direction, prompting skill required direction finding correct
answers.
Very effective method of verifying the students is a method of practicing, for
example, at laboratory studies: the practice of working with instruments and devices of
biochemical laboratory, practice of proper use of laboratory equipment, etc.
In didactic practice, there is increasingly using didactic tests those are
standardized set of tasks to specific educational material through which define the level
of mastery. Tests allow you to objectively assess the level of mastery of theoretical
knowledge, practical skills and abilities.
For training purposes, tests are divided into four types:
• verification of knowledge (facts, concepts, laws, theories), ie knowledge of
information that was necessary to continue to remember and now reproduce. The
main thing here is the reproduction of knowledge;
• identify skills to perform certain mental actions based on acquired knowledge.
Requires ability to solve common tasks;
• identify their own skills to make a critical analysis of the material studied;
• identifying the skills students creatively use the knowledge in solving non-routine
tasks.
In higher education institutions, there are also beginning to be used for
monitoring and assessing students programmable control. This broad possibility give
computers that provide immediate feedback between the response of the trained and
programmed learning material, allow immediately get information about the level of
response.
Method of machine (programmable) control is carried out by means of electronic
computers and control programs. The computer is the most objective controller in the
study all subjects. Software controls are made up according to the method of control of
programmed exercises; answers are typed as numbers or formulas. However, the
machine can not take into account the psychological characteristics of the student; can
not completely replace the teacher, especially in a timely manner to assist him in case of
difficulties with choosing the correct answer.
Method of test control can be out of engine (under condions of not using
computer) and engine (under condions of using computer). The basis of such control are
13
tests - special tasks performance (or failure) of which indicates the presence (or
absence) in the students certain knowledge, skills.
To control the quality of the knowledge and skills students study subject
"Biochemistry of Animals with Fundamentals of Physical and Colloidal Chemistry"
traditionally used: individual interviews, tests, modular work, colloquia, tests, exams
etc.
11. Distribution of points that get students. Evaluation of the student is in
accordance with the provisions of "On the examinations and tests NUBiP in
Ukraine" 27.02.2019. The protocol number 6 from the table. 1.
12.
Сума балів National estimation
Exam Test
90-100 “Excellent” credited
74-89 “Good”
60-73 “Satisfactory”
0-59 “Unsatisfactory” not credited
Rating from attestation is determined on a 100 ball scale and includes rating from a
test, that calculation Rtest. = 30.0 points, which settles accounts after a formula:
Rat.= 0.3 ∙ Rtest.
For determination of the real rating from discipline it is necessary to make the
marks collected during an educational semester:
R = 70 + 30 = 100 points.
14
11. Methodical maintenance
1. Methodical recommendations to laboratory classes on «Biochemistry of animals
with fundamentals of physical and colloidal chemistry» for students of Faculty of
Veterinary Medicine; Part I; Physico-chemical methods in biochemical
investigation / С.Д. Мельничук, Л.Г. Калачнюк // Методичні рекомендації. К:
Видавничий центр НУБіП України, 2013. – 149 с.
2. Методичні рекомендації до виконання лабораторних робіт з дисципліни:
«Біохімія тварин з основами фізичної і колоїдної хімії» для студентів
факультету ветеринарної медицини. Методичні рекомендації / С.Д.
Мельничук, Л.Г. Калачнюк, Г.І. Калачнюк, Л.В. Кліх. К: Видавничий центр
НУБіП України, 2013. – 148 с.
3. Закон України "Про вищу освіту" // Держава і право. – 2002. – № 43.
4. Національна доктрина розвитку освіти // Освіта України– 2002. – 23 квітня.
5. Алексюк А. М. Педагогіка вищої школи. Історія. Теорія. Курс лекцій:
модульне навчання. – К., 1993.
6. Васянович Г.П. Педагогіка вищої школи Навч.‐ метд. посібн. – Львів, 2000.
7. Кузьмінський А.І. Підагогіка вищої школи.: Навч. посіб. – К., 2005.
8. Педагогіка вищої школи. Навчальний посібник. – Одеса: ПДПУ імені К.Д.
Ушинського, 2002.
9. Фіцула М.М. Педагогіка вищої школи: Навч. посіб. – К., 2006.
10. Шейко В.М., Кушнаренко Н.М. Організація та методика
науково‐дослідницької діяльності: Підручник. – К., 2006.
11. П’ятакова Г.П. Технологія інтерактивного навчання у вищій школі.
Навчально ‐ метод. посібник. – Львів, 2008
12. Дичківська І.М. Основи педагогічної інноватики навчальний посібник. –
Рівне: РДПУ. 2001. – 233 с.
13. Дичківська І.М. Інноваційні педагогічні технології. Навч. посібник. – К.:
Академ.видав., 2004. – 352 с.
14. Андрущенко В. Високі педагогічні технології / В. Андрущенко, В. Олексенко
// Вища освіта України. - 2007. - № 2. - С. 70 -76.
15. Пінчук О. Проблема визначення мультимедіа в освіті: технологічний аспект //
Нові технології навчання. - К., 2007. - Вип. 46. - С. 55 - 58.
16. Гончаров С.М. Інтерактивні технології навчання в кредитно-модульній
системі організації навчального процесу: Навчально-методичний посібник. -
Рівне: НУВГП, 2006. - 172 с.
17. Бабанский Ю.К., Поташник М.М. Оптимизация педагогического процесса: В
вопросах и ответах. - 2-е узд., переработанное и доп. - К., 1984.
18. Вища освіта України і Болонський процес: Навчальний посібник / За
редакцією В.Г. Кременя, Авторський колектив: М.Ф. Степко, Я.Я. Болюбаш,
В.Д. Шинкарук, В.В. Грубінко, І.І. Бабин. - Тернопіль: Навчальна книга -
Богдан, 2004. - 384 с.
19. Болюбаш Я.Я. Організація навчального процесу у вищих закладах освіти:
Навч. посібник для слухачів закладів підвищення кваліфікації системи вищої
освіти.— К.: ВВП «КОМПАС», 1997.— 64с.
15
12. Recommended Literature
- Basic;
1. Біохімія: практикум / Д.О. Мельничук, С.Д. Мельничук, Л.Г. Калачнюк, Г.І.
Калачнюк. За загальною редакцією академіка НАН України і НААН Д.О.
Мельничука (рекомендовано Міністерством освіти і науки, молоді та спорту
України, лист № 1/11-16887 від 30.10.2012) - К: ВЦ НУБіП України, 2012, 528 с.
2. Маршалл В.Дж., Бангерт С.К. Клиническая химия. 6-е изд.: Пер. с англ. М:
Бином, 2011. – 408 с.
3. Фаллер Дж.М., Шилдс Д. Молекулярная биология клетки. Руководство для
врачей. Пер. с англ. М: Бином-Пресс, 2011. – 256 с.
4. Кольман Я., Рем К.-Г. Наглядная биохимия. 3-е изд.: Пер. с нем. М.: Мир, 2009.
− 469 с.
5. Марри Р., Греннер Д., Мейс П., Родуэлл В. Биохимия человека – М.: Мир, 2009.
− Т. 1. − 381 с.
6. Марри Р., Греннер Д., Мейс П., Родуэлл В. Биохимия человека – М.: Мир, 2009.
− Т. 2. − 414 с.
7. Николаев А.Я. Биологическая химия. 3-е изд., перераб и доп. − М.:
Медицинское информационное агенство. − 2007. − 568 с.
8. Губський Ю.І. Біологічна хімія. Київ – Вінниця: Нова книга, 2007. – 655 с.
9. Nelson D.L., Cox M.M. Lehninger Principles of Biochemistry (Fourth Edition) – W.
H. Freeman Publishers. 2004.-1124р.
10. Berg J.M., Tymoczko J.L., Stryer L. Biochemistry. – New York: W H Freeman; 2002.
1515 p.
11. Губський Ю.І. Біоорганічна хімія. Київ – Вінниця: Нова книга, 2007. – 431 с.
– Supplemental.
1. Ленинджер А. Основы биохими (в 3-х томах), Москва: Мир, 1985.
2. Губський Ю.І. Біологічна хімія. Київ – Вінниця: Нова книга, 2007. – 655 с.
3. Губський Ю.І. Біоорганічна хімія. Київ – Вінниця: Нова книга, 2007. – 431 с.
4. Біологічна хімія з основами фізичної та колоїдної хімії (лабораторно-
практичні заняття), укладачі: Д.О. Мельничук та ін. Київ, 1998. – 147 с.
5. Практикум з органічної хімії, під редакцією Д.О. Мельничука. Київ:
Видавничий центр НАУ, 2002. – 133 с.
6. Стрельцов О.А., Мельничук Д.О., Снітинський В.В. та ін. Фізична і
колоїдна хімія. Львів: Ліга-Прес, 2002. – 456 с.
7. Шевряков М.В., Яковенко Б.В., Явоненко О.Ф. Практикум з біологічної хімії.
Суми: Університетська книга, 2003. – 203 с.
8. Кононський О.І. Біохімія тварин. Київ: Вища шк., 2006. – 454 с.
9. Кононський О.І. Органічна хімія. Київ: Дакор, 2003. – 567 с.
10. Кононський О.І. Органічна хімія. Практикум. Київ: Вища школа, 2002. – 247
с.
11. Кононский А.И. «Физическая и коллоидная химия». К:Вища школа. 1986.
16
13. Information Resources
1. Web-pages of scientific journals: Ukrainian biochemical journal, Animal biology, etc.
2. "Wikipedia" Web-page and other Internet sources.
The work program is consistent with the basic training plan for higher education
in the field of "Veterinary Medicine" according to the “MEB”, namely: "Biochemistry
is a link between the inanimate world of chemistry and the living world of biology. The
content of the discipline should provide the veterinary student with a broad
understanding of the structure and function of basic biological molecules (eg, proteins,
lipids, carbohydrates, DNA, RNA, as well as metabolic processes and regulation). It is
necessary to highlight the comparative features among the species of animals that are of
particular importance to the countries participating in the “MEB”.